The effects ofN-ethylmaleimide on extracellularly and intracellularly generated chemiluminescence in neutrophils indicate that the rate of deactivation of NADPH-oxidase is higher when the oxidase system is localized on the plasma membrane than when it is localized on the phagosomal membrane

1991 ◽  
Vol 6 (2) ◽  
pp. 81-86 ◽  
Author(s):  
Claes Dahlgren ◽  
Tommy Sundqvist
Keyword(s):  
Plasma Membrane ◽  
Nadph Oxidase ◽  
Oxidase System ◽  
Phagosomal Membrane

scholarly journals Membrane Dynamics and Organization of the Phagocyte NADPH Oxidase in PLB-985 Cells

2020 ◽  
Vol 8 ◽  
Author(s):  
Jérémy Joly ◽  
Elodie Hudik ◽  
Sandrine Lecart ◽  
Dirk Roos ◽  
Paul Verkuijlen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Nadph Oxidase ◽  
Proteolytic Enzymes ◽  
Super Resolution ◽  
Membrane Dynamics ◽  
Small Gtpase ◽  
Human Neutrophils ◽  
Number Of Clusters ◽  
Phagocyte Nadph Oxidase ◽  
Phagosomal Membrane

Neutrophils are the first cells recruited at the site of infections, where they phagocytose the pathogens. Inside the phagosome, pathogens are killed by proteolytic enzymes that are delivered to the phagosome following granule fusion, and by reactive oxygen species (ROS) produced by the NADPH oxidase. The NADPH oxidase complex comprises membrane proteins (NOX2 and p22phox), cytoplasmic subunits (p67phox, p47phox, and p40phox) and the small GTPase Rac. These subunits assemble at the phagosomal membrane upon phagocytosis. In resting neutrophils the catalytic subunit NOX2 is mainly present at the plasma membrane and in the specific granules. We show here that NOX2 is also present in early and recycling endosomes in human neutrophils and in the neutrophil-like cell line PLB-985 expressing GFP-NOX2. In the latter cells, an increase in NOX2 at the phagosomal membrane was detected by live-imaging after phagosome closure, probably due to fusion of endosomes with the phagosome. Using super-resolution microscopy in PLB-985 WT cells, we observed that NOX2 forms discrete clusters in the plasma membrane. The number of clusters increased during frustrated phagocytosis. In PLB-985NCF1ΔGT cells that lack p47phox and do not assemble a functional NADPH oxidase, the number of clusters remained stable during phagocytosis. Our data suggest a role for p47phox and possibly ROS production in NOX2 recruitment at the phagosome.

Reactive oxygen species produced via plasma membrane NADPH oxidase regulate anthocyanin synthesis in apple peel

Planta ◽  
2014 ◽  
Vol 240 (5) ◽  
pp. 1023-1035 ◽  
Author(s):  
Jiangli Zhang ◽  
Changsheng Chen ◽  
Di Zhang ◽  
Houhua Li ◽  
Pengmin Li ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Plasma Membrane ◽  
Nadph Oxidase ◽  
Reactive Oxygen ◽  
Anthocyanin Synthesis ◽  
Oxygen Species ◽  
Apple Peel

Topics in Chronic Granulomatous Disease

PEDIATRICS ◽  
1991 ◽  
Vol 88 (1) ◽  
pp. 183-185
Author(s):  
SHIGENOBU UMEKI
Keyword(s):  
Nadph Oxidase ◽  
Chronic Granulomatous Disease ◽  
Host Defense ◽  
Superoxide Anion ◽  
Fungal Infections ◽  
Regulatory Elements ◽  
Granulomatous Disease ◽  
Phagocytic Cells ◽  
Oxidase System ◽  
Membrane Bound

To the Editor.— Such phagocytic cells as neutrophils and macrophages are crucial elements in the host defense against bacterial [See table in the PDF file] and fungal infections. Microbicidal activity depends to a large extent on NADPH oxidase system, which can be activated by stimuli (bacteria, fungi) and which generates the superoxide anion and other highly reactive forms of reduced oxygen.1,2 The neutrophil NADPH oxidase system is composed functionally of membrane-bound catalytic components (which consist of at least two constituents, the low potential cytochrome b5583-5 and flavoprotein5) and soluble cytosolic components6,7 which participate as either catalytic or regulatory elements.

Role of the Vascular NADH/NADPH Oxidase System in Atherosclerosis

2006 ◽  
Vol 902 (1) ◽  
pp. 241-248 ◽  
Author(s):  
MITSUHIRO YOKOYAMA ◽  
NOBUTAKA INOUE ◽  
SEINOSUKE KAWASHIMA
Keyword(s):  
Nadph Oxidase ◽  
Oxidase System

Abstract 361: Cyclophilin A Mediates Angiotensin II--Stimulated NADPH Oxidase Activation in Vascular Smooth Muscle Cells

2012 ◽  
Vol 32 (suppl_1) ◽  
Author(s):  
Nwe Nwe Soe ◽  
Mark Sowden ◽  
Patrizia Nigro ◽  
Bradford C Berk
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Nadph Oxidase ◽  
Smooth Muscle Cells ◽  
Fold Increase ◽  
Muscle Cells ◽  
Dependent Manner ◽  
Ang Ii ◽  
Membrane Translocation ◽  
Ppiase Activity

Objective: Cyclophilin A (CyPA) is a ubiquitously expressed cytosolic protein that possesses PPIase activity and scaffold function. CyPA regulates Angiotensin II (Ang II) induced reactive oxygen species (ROS) production in vascular smooth muscle cells. However, the mechanism of this CyPA regulation remains unclear. We hypothesized that CyPA regulates plasma membrane translocation of NADPH oxidase cytosolic subunit, p47phox, which is required for NADPH oxidase structural organization and activity. Methods and results: Immunofluorescence studies in rat aortic smooth muscle cells revealed that CyPA translocated from the cytosol to the plasma membrane in response to Ang II in a time dependent manner with a peak at 10min (46.4±5.4 fold increase). Mouse Aortic Smooth Muscle Cells (MASM) were isolated from mice lacking CyPA (CyPA-/-) and wild type controls (WT), treated with Ang II (100nM) and immunofluorescence analysis was performed. Ang II induced p47phox plasma membrane translocation at 10min in WT mice. However, p47 phox translocation was significantly inhibited in CyPA -/- MASM. CyPA and p47phox colocalized at the plasma membrane in response to Ang II. Further analysis using subcellular fractionation studies confirmed that Ang II induced p47phox plasma membrane translocation was inhibited in CyPA -/- MASM compared to WT (1.2±2.7 vs 4.3±3.4 fold increase). Coimmunoprecipitation analyses confirmed that Ang II increased CyPA association with p47phox in a time dependent manner (2.5±3.4 fold increase at 10min). Finally, pretreatment with the PPIase activity inhibitor, cyclosporine A (1uM), could not inhibit CyPA association with p47phox and CyPA mediated p47phox translocation to the plasma membrane. Conclusion: These data suggest that Ang II promotes an association between CyPA and p47phox that enhances plasma membrane translocation of p47phox. This is proposed to increase the NADPH oxidase activity thereby increasing cellular ROS production. This process is independent of the PPIase activity of CyPA. Therefore, inhibition of the CyPA and p47phox association could be a future therapeutic target for Ang II induced ROS regulated cardiovascular diseases such as atherosclerosis and abdominal aortic aneurysm formation.

scholarly journals Melatonin improves rice salinity stress tolerance by NADPH oxidase‐dependent control of the plasma membrane K + transporters and K + homeostasis

2020 ◽  
Vol 43 (11) ◽  
pp. 2591-2605 ◽  
Author(s):  
Juan Liu ◽  
Sergey Shabala ◽  
Jing Zhang ◽  
Guohui Ma ◽  
Dandan Chen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Nadph Oxidase ◽  
Stress Tolerance ◽  
Salinity Stress ◽  
Salinity Stress Tolerance
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